title: Spectroscopic study on the interaction of Trypsin with Bicyclol and analogs.
abstract: The interactions between Trypsin and Bicyclol or analogs (Bifendate, I, II and III) were investigated by spectrophotometric methods. It was found that Bicyclol or analogs had strong ability to quench the intrinsic fluorescence of Trypsin by a static quenching procedure. The binding constants were obtained at three temperatures. The thermodynamics parameters reveal that the hydrophobic and electrostatic interactions play an important role in the interaction. Results showed that the microenvironments of tryptophan residue of Trypsin were disturbed by the analogs. Results indicated that Bifendate was the strongest quencher among five compounds.
authors.affiliation: College of Chemistry and Molecular Engineering, Zhengzhou University, 100 Science Avenue, Zhengzhou 450001, China.
authors.forename: Wu
authors.initials: W
authors.lastname: He
authors.forename: Huanjing
authors.initials: H
authors.lastname: Dou
authors.forename: Lu
authors.initials: L
authors.lastname: Zhang
authors.forename: Lvjing
authors.initials: L
authors.lastname: Wang
authors.forename: Ruiyong
authors.initials: R
authors.lastname: Wang
authors.forename: Junbiao
authors.initials: J
authors.lastname: Chang
mesh_terms: D000998:Antiviral Agents / Q000737:chemistry / Q000378:metabolism*; D001713:Biphenyl Compounds / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D013050:Spectrometry, Fluorescence; D013816:Thermodynamics; D014357:Trypsin / Q000378:metabolism*
chemical_list: D000998:Antiviral Agents; D001713:Biphenyl Compounds; C477843:bicyclol; D014357:Trypsin
keywords: Analogs; Bicyclol; Interaction; Trypsin